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2.3.3.16: citrate synthase (unknown stereospecificity)

This is an abbreviated version!
For detailed information about citrate synthase (unknown stereospecificity), go to the full flat file.

Word Map on EC 2.3.3.16

Reaction

acetyl-CoA
+
H2O
+
oxaloacetate
=
citrate
+
CoA

Synonyms

bifunctional citrate synthase/2-methylcitrate synthase, CCNA_01983, CIT1, CitA, citrate condensing enzyme, citrate oxaloacetate-lyase (CoA-acetylating), citrate oxaloacetate-lyase, CoA-acetylating, citrate synthase, citrate synthase Cit1, citrate synthase/2-methylcitrate synthase, citrate synthetase, citric synthase, citric-condensing enzyme, citrogenase, CitZ, CS, CS1, CS2, CS3, CS4, CSI, CSY, CSY4, CTS, EC 4.1.3.7, gltA, GltA2, MCS, mitochondrial citrate synthase, mmgD, More, Msed_1522, oxalacetic transacetase, oxaloacetate transacetase, peroxisomal citrate synthase, Rv0896, SbnG, Si-citrate synthase, sll0401, SSO2589, St0589, St1805, synthase, citrate, TTHA1343, type II citrate synthase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.16 citrate synthase (unknown stereospecificity)

Crystallization

Crystallization on EC 2.3.3.16 - citrate synthase (unknown stereospecificity)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with oxaloacetate and inhibitor carboxymethyldethia-coenzyme A. The surface of citrate synthase is decoreated abundantly with basic side chains and this constellation is stable in varied pH environments
structure of apo-CSY4, at 2.69 A resolution. Dimerization of AtCSY4 is mainly mediated by alpha-helices H6, H7, H8, H12 and H13 from one molecule upon interaction with the corresponding alpha-helices from another molecule. The N-terminal (H1, H2, S1 and S2) and C-terminal (H20 and S6) regions are also important in dimerization
structural modeling and functional annotation
hanging drop vapour diffusion method, from 2-2.3 M ammonium sulfate, 2% v/v polyethylene glycol 400, 0.1 M HEPS, pH 6.0, X-ray diffraction analysis, structure determination and modeling: 3 identical dimer units arranged about a central 3-fold axis
hanging-drop vapour-diffusion method from 2.0-2.2 M ammonium sulfate, 2% PEG 400, and 0.1 M Na-HEPES at pH 6.0. the NADH-bound form of mutant R109L is obtained by soaking a variant crystal in a solution containing 1.22 mM NADH, 2.8 M ammonium sulfate, 2% polyethylene glycol 400 and 0.1 M Na-Hepes at pH 6.0
-
crystal structure at 1.7 A resolution. Like other Type-I CS, citrate synthase functions as a dimer and each monomer consists of a large domain and a small domain. The oxaloacetate binding site locates at the cleft between the two domains, and the active site is more closed upon binding of the oxaloacetate substrate than binding of the citrate product
structure of the complex with acetyl-CoA, to 1.72 A resolution. Residues His218, His258, and Asp313 are located at the active site. The pantothenic acid part of acetyl-CoA is stabilized by the main chain of Gly255 and side chain of Asp313 by direct and water mediated hydrogen binding networks. The acetyl group in the acetyl-CoA tail is stabilized by two carbonyl group at the main chain of Pro216 and Gly219 through water-mediated hydrogen bonds
hanging drop vapor diffusion method, using 0.2 M magnesium chloride hexahydrate, 0.1M Tris pH 8.5, 3.4 M 1,6-hexandiol
crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus
-
hanging drop vapour diffusion method, room temperature, 2 mg/ml protein concentration, precipitation by 0.1 M sodium citrate and 0.1 M ammonium phosphate, 20 mM Tris-HCl, pH 8.0, 25 mM KCl, x-ray structure analysis, structural basis of high thermostability
comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
hanging-drop vapour diffusion method, 2.7 A resolution
wild type enzyme bound to calcium by the hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 M imidazole (pH 9.0), and 4-6% (w/v) PEG 8000, and an active site variant E151Q in complex with oxaloacetate by the sitting drop vapor diffusion method, using 5% (v/v) tascimate (pH 7.0), 0.1 M HEPES (pH 7.0), 10% (w/v) PEG monomethyl ether 5000 and about 40 mM guanidine hydrochloride
structure at 2.0 A resolution. Residues His184, His259, Arg268, Arg339, and Arg359', which are important residues for substrate binding, are exposed to the inner surface of the open cleft
structure at 2.7 A resolution. Putative substrate-binding residues His180, His215, His254, Arg263, Arg335, and Arg354' are structurally conserved
pH 7.8, PEG 3350, aspartame, benzamidine, cysteamine
comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus
-
hanging drop vapor diffusion method, using 0.1 M CHES pH 9.5, 12% (w/v) PEG 4000, 1 mM oxaloacetate
-
unliganded form and the enzyme in complex with oxaloacetate. Oxaloacetate is most likely the quencher of tryptophan fluorescence with the oxaloacetate carbonyl as the electron acceptor
-
comparison of rigidity in citrate synthases from thermophiles to investgate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein